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细菌中苏氨酸脱水酶的分子进化

Molecular evolution of threonine dehydratase in bacteria.

作者信息

Yu Xuefei, Li Ye, Wang Xiaoyuan

机构信息

State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China ; Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi, China.

出版信息

PLoS One. 2013 Dec 4;8(12):e80750. doi: 10.1371/journal.pone.0080750. eCollection 2013.

Abstract

Threonine dehydratase converts L-threonine to 2-ketobutyrate. Several threonine dehydratases exist in bacteria, but their origins and evolutionary pathway are unknown. Here we analyzed all the available threonine dehydratases in bacteria and proposed an evolutionary pathway leading to the genes encoding three different threonine dehydratases CTD, BTD1 and BTD2. The ancestral threonine dehydratase might contain only a catalytic domain, but one or two ACT-like subdomains were fused during the evolution, resulting BTD1 and BTD2, respectively. Horizontal gene transfer, gene fusion, gene duplication, and gene deletion may occur during the evolution of this enzyme. The results are important for understanding the functions of various threonine dehydratases found in bacteria.

摘要

苏氨酸脱水酶将L-苏氨酸转化为2-酮丁酸。细菌中存在几种苏氨酸脱水酶,但其起源和进化途径尚不清楚。在这里,我们分析了细菌中所有可用的苏氨酸脱水酶,并提出了一条导致编码三种不同苏氨酸脱水酶CTD、BTD1和BTD2的基因的进化途径。原始的苏氨酸脱水酶可能仅包含一个催化结构域,但在进化过程中分别融合了一个或两个ACT样亚结构域,从而产生了BTD1和BTD2。在这种酶的进化过程中可能发生水平基因转移、基因融合、基因复制和基因缺失。这些结果对于理解细菌中发现的各种苏氨酸脱水酶的功能很重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba3d/3851459/aaf0df97ebad/pone.0080750.g001.jpg

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